Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Major vault protein  

UniProtKB / Swiss-Prot ID :  MVP_HUMAN

Gene Name (Synonyms) : 
MVP, LRP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus, nuclear pore complex. Note=5% found in the nuclear pore complex. Translocates from the nucleus to the cytoplasm upon EGF treatment. 

Protein Function :  Required for normal vault structure. Vaults are multi- subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo- cytoplasmic transport. Down-regulates INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases. 

Protein Sequence MATEEFIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPMRMVTVPPRHYCTVANPVSRDAQ...
Predicted Secondary Structure CCCCCCEEEECCCEEEEEEECCCCEEEEEECCCCEEEECCCEEECCCCCEEEECCCCEEEEECCCEECCC...
Protein Variant
LocationDescription
635V -> I (in dbSNP:rs35916172). VAR_050179
651R -> Q (in dbSNP:rs3764944). VAR_050180
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATEEF
---CCCCCC
24.58UniProtKB
Link-
13PhosphotyrosineRIPPYHYIH
EECCCEEEE
11.25PhosphoELM
Link-
13PhosphotyrosineRIPPYHYIH
EECCCEEEE
11.25Phosphositeplus
Link-
13Phosphotyrosine.RIPPYHYIH
EECCCEEEE
11.25UniProtKB
Link-
15PhosphotyrosinePPYHYIHVL
CCCEEEEEE
6.20HPRD
Link-
15PhosphotyrosinePPYHYIHVL
CCCEEEEEE
6.20PhosphoELM
Link-
15PhosphotyrosinePPYHYIHVL
CCCEEEEEE
6.20Phosphositeplus
Link-
15Phosphotyrosine.PPYHYIHVL
CCCEEEEEE
6.20UniProtKB
Link-
370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VPSAKVEVV
CCCCEEEEE
43.18Phosphositeplus
Link-
444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KDTAKSLQP
CCCCCCCCC
54.51Phosphositeplus
Link-
445PhosphoserineDTAKSLQPL
CCCCCCCCC
29.76Phosphositeplus
Link-
445PhosphoserineDTAKSLQPL
CCCCCCCCC
29.76SysPTM
Link-
674Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EAAAKHEAQ
CHHHHHHHH
36.93Phosphositeplus
Link-
747Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QAKLKAQAL
HHHHHHHHH
37.43Phosphositeplus
Link-
830PhosphothreonineGLKSTLITD
CCCEEEEEC
22.16HPRD
Link-
833PhosphothreonineSTLITDGST
EEEEECCCC
37.10HPRD
Link-
864PhosphoserineRRVASGPSP
CCCCCCCCC
48.67Phosphositeplus
Link-
873PhosphoserineGEGISPQSA
CCCCCCCCC
27.95HPRD
Link-
873PhosphoserineGEGISPQSA
CCCCCCCCC
27.95Phosphositeplus
Link-
876PhosphoserineISPQSAQAP
CCCCCCCCC
26.23HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ESR1_HUMANin vitro
in vivo
HPRD:05475HPRD9628887
PTEN_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:05475HPRD12177006
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND MASSSPECTROMETRY.
"The major vault protein is a novel substrate for the tyrosinephosphatase SHP-2 and scaffold protein in epidermal growth factorsignaling.";
Kolli S., Zito C.I., Mossink M.H., Wiemer E.A.C., Bennett A.M.;
J. Biol. Chem. 279:29374-29385(2004).
Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES, MASS SPECTROMETRY, INTERACTIONWITH PTPN11, SUBCELLULAR LOCATION, AND FUNCTION.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures